ID D9Q1U8_ACIS3 Unreviewed; 460 AA.
AC D9Q1U8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN OrderedLocusNames=ASAC_0880 {ECO:0000313|EMBL:ADL19286.1};
OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS 345-15).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus.
OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL19286.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL19286.1, ECO:0000313|Proteomes:UP000000346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC {ECO:0000313|Proteomes:UP000000346};
RX PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT a new order, Acidilobales, and suggests an important ecological role in
RT terrestrial acidic hot springs.";
RL Appl. Environ. Microbiol. 76:5652-5657(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|RuleBase:RU000504};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; CP001742; ADL19286.1; -; Genomic_DNA.
DR AlphaFoldDB; D9Q1U8; -.
DR STRING; 666510.ASAC_0880; -.
DR KEGG; asc:ASAC_0880; -.
DR eggNOG; arCOG04120; Archaea.
DR HOGENOM; CLU_015439_0_2_2; -.
DR InParanoid; D9Q1U8; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000000346; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:ADL19286.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000346};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:ADL19286.1}.
FT DOMAIN 4..320
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 350..447
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 460 AA; 50477 MW; F66E222FE8F04CDF CRC64;
MKRLAKIMVT MGPSTLDYAI VRRMMSAGAD GFRINMSHGD EKQWATFLEL IDKASQELGV
HVAKVADLEG PRVRLGEFQG VDIAPGQQVR FKYKDAQGEG IPVDNRAFFA SLERGDRVLV
DDGKVVLSVE DIERDSATLR VISGQRLEPR KGVVLAGKEY DLPPVTEKDL QNMKFIAANN
FDYVMASFVR SARHVEIIRK ALSDAGAKDV KLLAKIETPS GVNNIDSILD VVDGIVVARG
DLGMHFPLED IPVIQRRIIE AARRKLKPVI LATEIFMSMI ERPLPTRGEI SDVYAGIEEG
VDGFLVTSET SIGKYPAEVV SWLSRVIEEA NKNVRPRRVD QLTSSLESRI SRGVVEMAQN
VGASVVVYAH DFDVARLISA FRPGTSIYVG VPTTQLARQL SLLWGTVPVV VGPADSEEQG
LEATEKELES KGITGPGSLL VELSWTPDRS TAVVKVKQVF
//
